| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2000PNAS...97.3288W |
| P356 | DOI | 10.1073/PNAS.97.7.3288 |
| P8608 | Fatcat ID | release_k73rf7goi5agfelf7flvoledcm |
| P932 | PMC publication ID | 16231 |
| P698 | PubMed publication ID | 10725404 |
| P2093 | author name string | W R Atchley | |
| W. R. Atchley | |||
| K R Wollenberg | |||
| K. R. Wollenberg | |||
| P2860 | cites work | CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice | Q24286950 |
| Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition | Q24532538 | ||
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| A natural classification of the basic helix-loop-helix class of transcription factors | Q24642491 | ||
| Correlated mutations and residue contacts in proteins | Q25891592 | ||
| The neighbor-joining method: a new method for reconstructing phylogenetic trees | Q25939010 | ||
| Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation | Q27731319 | ||
| Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain | Q27732150 | ||
| Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 A resolution | Q27759142 | ||
| A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences | Q27860580 | ||
| The rapid generation of mutation data matrices from protein sequences | Q27860880 | ||
| Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer | Q28238671 | ||
| Caloramator viterbensis sp. nov., a novel thermophilic, glycerol-fermenting bacterium isolated from a hot spring in Italy | Q29642131 | ||
| Constructing amino acid residue substitution classes maximally indicative of local protein structure | Q30424569 | ||
| Compensating changes in protein multiple sequence alignments | Q34340790 | ||
| Positional dependence, cliques, and predictive motifs in the bHLH protein domain | Q44871206 | ||
| Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution. | Q52262566 | ||
| Statistical tests of models of DNA substitution | Q52402132 | ||
| Modeling residue usage in aligned protein sequences via maximum likelihood | Q71852465 | ||
| An analysis of simultaneous variation in protein structures | Q73439289 | ||
| P433 | issue | 7 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | phylogenetics | Q171184 |
| P1104 | number of pages | 4 | |
| P304 | page(s) | 3288-3291 | |
| P577 | publication date | 2000-03-01 | |
| 2000-03-28 | |||
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Separation of phylogenetic and functional associations in biological sequences by using the parametric bootstrap | |
| P478 | volume | 97 |
| Q38177613 | A survey on prediction of specificity-determining sites in proteins |
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| Q34455146 | Accurate simulation and detection of coevolution signals in multiple sequence alignments |
| Q34957027 | Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases |
| Q33403910 | Analysing the origin of long-range interactions in proteins using lattice models |
| Q35770682 | Assembly constraints drive co-evolution among ribosomal constituents |
| Q50884788 | Co-evolutionary constraints of globular proteins correlate with their folding rates. |
| Q40538411 | Codon-level information improves predictions of inter-residue contacts in proteins by correlated mutation analysis |
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| Q35754130 | Coevolutionary analyses require phylogenetically deep alignments and better null models to accurately detect inter-protein contacts within and between species |
| Q81484406 | Coevolutionary patterns in cytochrome c oxidase subunit I depend on structural and functional context |
| Q36251118 | Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication |
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| Q30350655 | Context dependence and coevolution among amino acid residues in proteins. |
| Q30375462 | Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information. |
| Q33467381 | Correlated mutation analysis on the catalytic domains of serine/threonine protein kinases |
| Q30011142 | Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis |
| Q34410131 | Coupled mutation finder: a new entropy-based method quantifying phylogenetic noise for the detection of compensatory mutations |
| Q30374414 | Covariation Is a Poor Measure of Molecular Coevolution. |
| Q33389536 | Detecting coevolution without phylogenetic trees? Tree-ignorant metrics of coevolution perform as well as tree-aware metrics |
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| Q35716090 | Did α-Synuclein and Glucocerebrosidase Coevolve? Implications for Parkinson's Disease |
| Q39204291 | Direct coevolutionary couplings reflect biophysical residue interactions in proteins |
| Q24627074 | Direct-coupling analysis of residue coevolution captures native contacts across many protein families |
| Q21563484 | Disentangling direct from indirect co-evolution of residues in protein alignments |
| Q28469282 | Distinguishing functional amino acid covariation from background linkage disequilibrium in HIV protease and reverse transcriptase |
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| Q35919894 | Phylogenetic analysis and classification of the fungal bHLH domain |
| Q47222847 | Power law tails in phylogenetic systems |
| Q28477179 | Prevalence of epistasis in the evolution of influenza A surface proteins |
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| Q30412218 | Sequence coevolution between RNA and protein characterized by mutual information between residue triplets |
| Q33772010 | Solving the protein sequence metric problem |
| Q37173119 | Spectral analysis of sequence variability in basic-helix-loop-helix (bHLH) protein domains |
| Q33523274 | Structural and functional roles of coevolved sites in proteins |
| Q33518462 | Trade-off between positive and negative design of protein stability: from lattice models to real proteins |
| Q30369660 | Using inferred residue contacts to distinguish between correct and incorrect protein models |
| Q37037782 | Why should we care about molecular coevolution? |
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